Identification and characterization of a novel elastase inhibitor from Hirudinaria manillensis.
10.1016/S1875-5364(21)60054-7
- Author:
Kuan-Hong XU
1
;
Meng ZHOU
2
;
Fei-Long WU
3
;
Xiao-Peng TANG
4
;
Qiu-Min LU
3
;
Ren LAI
3
;
Cheng-Bo LONG
5
Author Information
1. School of Life Sciences, University of Science and Technology of China, Hefei 230027, China.
2. Chongqing Institute of Medicinal Plant Cultivation, Nanchuan 408435, China.
3. Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences, Key Laboratory of Bioactive Peptides of Yunnan Province, Kunming Institute of Zoology, Kunming 650223, China; University of Chinese Academy of Sciences, Beijing 100049, China.
4. Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences, Key Laboratory of Bioactive Peptides of Yunnan Province, Kunming Institute of Zoology, Kunming 650223, China.
5. Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences, Key Laboratory of Bioactive Peptides of Yunnan Province, Kunming Institute of Zoology, Kunming 650223, China; University of Chinese Academy of Sciences, Beijing 100049, China. Electronic address: longchengbo@mail.kiz.ac.cn.
- Publication Type:Journal Article
- Keywords:
Anti-inflammation;
Elastase inhibitor;
HMEI-A;
Hirudinaria manillensis;
NET formation
- MeSH:
Amino Acid Sequence;
Animals;
Leeches/chemistry*;
Pancreatic Elastase/antagonists & inhibitors*;
Protease Inhibitors/pharmacology*;
Proteins
- From:
Chinese Journal of Natural Medicines (English Ed.)
2021;19(7):540-544
- CountryChina
- Language:English
-
Abstract:
A large number of protease inhibitors have been found from leeches, which are essential in various physiological and biological processes. In the curret study, a novel elastase inhibitor was purified and characterized from the leech of Hirudinaria manillensis, which was named HMEI-A. Primary structure analysis showed that HMEI-A belonged to a new family of proteins. HMEI-A exerted inhibitory effects on elastase and showed potent abilities to inhibit elastase with an inhibition constant (K
